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首页> 外文期刊>FEBS letters. >Kindlin-2 interacts with a-actinin-2 and p1 integrin to maintain the integrity of the Z-disc in cardiac muscles
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Kindlin-2 interacts with a-actinin-2 and p1 integrin to maintain the integrity of the Z-disc in cardiac muscles

机译:Kindlin-2与a-actinin-2和p1整合素相互作用以维持心肌中Z盘的完整性

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摘要

Kindlin-2, as an integrin-interacting protein, was known to be required for the maintenance of cardiac structure and function in zebrafish. However, the mechanism remains unclear. We found that Kindlin-2 interacts and colocalizes with alpha-actinin-2 at the Z-disc of mouse cardiac muscles and there Kindlin-2 also interacts with beta1 integrin. Knockdown of Kindlin-2 influences the association of beta1 integrin with alpha-actinin-2 and disrupts the structure of the Z-disc and leads to cardiac dysfunction. Our data indicated that Kindlin-2 is a novel alpha-actinin-2-interacting protein and plays an important role in the regulation of cardiac structure and function.
机译:Kindlin-2是一种整合素相互作用蛋白,是维持斑马鱼心脏结构和功能所必需的。但是,机制尚不清楚。我们发现Kindlin-2在小鼠心肌Z盘上与alpha-actinin-2相互作用并共定位,并且Kindlin-2也与beta1整联蛋白相互作用。敲低Kindlin-2会影响beta1整联蛋白与α-actinin-2的缔合,并破坏Z盘的结构并导致心脏功能障碍。我们的数据表明Kindlin-2是一种新型的alpha-actinin-2相互作用蛋白,在心脏结构和功能的调节中起着重要作用。

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